Structure of the factor xa-like trypsin variant triple-ala (tgpa) in complex with eglin C

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 34% strand (DSSP).

Ligands and binding sites

• CA · Calcium ion · metal · 2 copies · chains A, C
• CL · Chloride ion · ion · 2 copies · chains A, B, C
• GOL · Glycerol · additive · 9 copies · chains A, B, C, D
• EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

2 interfaces between chains.

• C–D · 1044 Ų buried · 20 hydrogen bonds · protein-protein
• A–B · 1030 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

• 4B2B · Structure of the factor Xa-like trypsin variant triple-Ala (TGPA) in complex with eglin C · the same entry in another collection · chain D against D, TM-score 1.00
• 1TNL · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain C against A, TM-score 0.99
• 1TNG · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.99
• 1TNI · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain C against A, TM-score 0.99
• 1TNJ · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain C against A, TM-score 0.99
• 1TNH · Prediction of novel serine protease inhibitors · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P00760
• Every structure of UniProt P01051
• Elsewhere: RCSB PDB 4B2B · PDBe 4B2B · UniProt P00760 · UniProt P01051